Quantitative analysis of the effective functional structure in yeast glycolysis.

The understanding of the effective functionality that governs the enzymatic self-organized processes in cellular conditions is a crucial topic in the post-genomic era. In recent studies, Transfer Entropy has been proposed as a rigorous, robust and self-consistent method for the causal quantification...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Ildefonso M De la Fuente, Jesus M Cortes
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/94373a32b5db44edaf219e68112d9704
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:94373a32b5db44edaf219e68112d9704
record_format	dspace
spelling	oai:doaj.org-article:94373a32b5db44edaf219e68112d97042021-11-18T07:26:30ZQuantitative analysis of the effective functional structure in yeast glycolysis.1932-620310.1371/journal.pone.0030162https://doaj.org/article/94373a32b5db44edaf219e68112d97042012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22393350/?tool=EBIhttps://doaj.org/toc/1932-6203The understanding of the effective functionality that governs the enzymatic self-organized processes in cellular conditions is a crucial topic in the post-genomic era. In recent studies, Transfer Entropy has been proposed as a rigorous, robust and self-consistent method for the causal quantification of the functional information flow among nonlinear processes. Here, in order to quantify the functional connectivity for the glycolytic enzymes in dissipative conditions we have analyzed different catalytic patterns using the technique of Transfer Entropy. The data were obtained by means of a yeast glycolytic model formed by three delay differential equations where the enzymatic rate equations of the irreversible stages have been explicitly considered. These enzymatic activity functions were previously modeled and tested experimentally by other different groups. The results show the emergence of a new kind of dynamical functional structure, characterized by changing connectivity flows and a metabolic invariant that constrains the activity of the irreversible enzymes. In addition to the classical topological structure characterized by the specific location of enzymes, substrates, products and feedback-regulatory metabolites, an effective functional structure emerges in the modeled glycolytic system, which is dynamical and characterized by notable variations of the functional interactions. The dynamical structure also exhibits a metabolic invariant which constrains the functional attributes of the enzymes. Finally, in accordance with the classical biochemical studies, our numerical analysis reveals in a quantitative manner that the enzyme phosphofructokinase is the key-core of the metabolic system, behaving for all conditions as the main source of the effective causal flows in yeast glycolysis.Ildefonso M De la FuenteJesus M CortesPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e30162 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ildefonso M De la Fuente Jesus M Cortes Quantitative analysis of the effective functional structure in yeast glycolysis.
description	The understanding of the effective functionality that governs the enzymatic self-organized processes in cellular conditions is a crucial topic in the post-genomic era. In recent studies, Transfer Entropy has been proposed as a rigorous, robust and self-consistent method for the causal quantification of the functional information flow among nonlinear processes. Here, in order to quantify the functional connectivity for the glycolytic enzymes in dissipative conditions we have analyzed different catalytic patterns using the technique of Transfer Entropy. The data were obtained by means of a yeast glycolytic model formed by three delay differential equations where the enzymatic rate equations of the irreversible stages have been explicitly considered. These enzymatic activity functions were previously modeled and tested experimentally by other different groups. The results show the emergence of a new kind of dynamical functional structure, characterized by changing connectivity flows and a metabolic invariant that constrains the activity of the irreversible enzymes. In addition to the classical topological structure characterized by the specific location of enzymes, substrates, products and feedback-regulatory metabolites, an effective functional structure emerges in the modeled glycolytic system, which is dynamical and characterized by notable variations of the functional interactions. The dynamical structure also exhibits a metabolic invariant which constrains the functional attributes of the enzymes. Finally, in accordance with the classical biochemical studies, our numerical analysis reveals in a quantitative manner that the enzyme phosphofructokinase is the key-core of the metabolic system, behaving for all conditions as the main source of the effective causal flows in yeast glycolysis.
format	article
author	Ildefonso M De la Fuente Jesus M Cortes
author_facet	Ildefonso M De la Fuente Jesus M Cortes
author_sort	Ildefonso M De la Fuente
title	Quantitative analysis of the effective functional structure in yeast glycolysis.
title_short	Quantitative analysis of the effective functional structure in yeast glycolysis.
title_full	Quantitative analysis of the effective functional structure in yeast glycolysis.
title_fullStr	Quantitative analysis of the effective functional structure in yeast glycolysis.
title_full_unstemmed	Quantitative analysis of the effective functional structure in yeast glycolysis.
title_sort	quantitative analysis of the effective functional structure in yeast glycolysis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/94373a32b5db44edaf219e68112d9704
work_keys_str_mv	AT ildefonsomdelafuente quantitativeanalysisoftheeffectivefunctionalstructureinyeastglycolysis AT jesusmcortes quantitativeanalysisoftheeffectivefunctionalstructureinyeastglycolysis
_version_	1718423488605192192

Quantitative analysis of the effective functional structure in yeast glycolysis.

Ejemplares similares